1. Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases
- Author
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Tiantian Su, Deshu Lin, James A. Wohlschlegel, Xu Wang, Zhensheng Gao, Qin Wang, Xiaohua Hu, Chentao Lin, Hsiaochi Huang, Yadi Chen, Huibo Ren, and Siyuan Liu
- Subjects
Photoreceptors ,0106 biological sciences ,0301 basic medicine ,Light ,Arabidopsis ,General Physics and Astronomy ,01 natural sciences ,Ubiquitin ,Cryptochrome ,Models ,Phosphorylation ,Polyubiquitin ,Multidisciplinary ,biology ,medicine.diagnostic_test ,Chemistry ,Cell biology ,Ubiquitin ligase ,Protein Binding ,Photoreceptors, Plant ,animal structures ,Science ,Ubiquitin-Protein Ligases ,Proteolysis ,Models, Biological ,Article ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,Light responses ,Genetics ,medicine ,Humans ,Blue light ,Arabidopsis Proteins ,HEK 293 cells ,Ubiquitination ,Plant ,General Chemistry ,Biological ,biology.organism_classification ,Cryptochromes ,HEK293 Cells ,030104 developmental biology ,Plant signalling ,Seedlings ,Mutation ,biology.protein ,sense organs ,010606 plant biology & botany - Abstract
Cryptochromes (CRYs) are photoreceptors or components of the molecular clock in various evolutionary lineages, and they are commonly regulated by polyubiquitination and proteolysis. Multiple E3 ubiquitin ligases regulate CRYs in animal models, and previous genetics study also suggest existence of multiple E3 ubiquitin ligases for plant CRYs. However, only one E3 ligase, Cul4COP1/SPAs, has been reported for plant CRYs so far. Here we show that Cul3LRBs is the second E3 ligase of CRY2 in Arabidopsis. We demonstrate the blue light-specific and CRY-dependent activity of LRBs (Light-Response Bric-a-Brack/Tramtrack/Broad 1, 2 & 3) in blue-light regulation of hypocotyl elongation. LRBs physically interact with photoexcited and phosphorylated CRY2, at the CCE domain of CRY2, to facilitate polyubiquitination and degradation of CRY2 in response to blue light. We propose that Cul4COP1/SPAs and Cul3LRBs E3 ligases interact with CRY2 via different structure elements to regulate the abundance of CRY2 photoreceptor under different light conditions, facilitating optimal photoresponses of plants grown in nature., The fate of proteins in cells is determined by not only synthesis but also degradation. Here Chen et al. show that degradation of the plant blue light receptor CRY2 is determined by two distinct E3 ubiquitin ligases, Cul4COP1/SPAs and Cul3LRBs, regulating the function of CRY2 under different light conditions.
- Published
- 2021